ID   B2GLV1_KOCRD            Unreviewed;      1274 AA.
AC   B2GLV1;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   04-NOV-2026, entry version 94.
DE   SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:BAG29292.1};
DE            EC=1.2.4.2 {ECO:0000313|EMBL:BAG29292.1};
GN   Name=sucA {ECO:0000313|EMBL:BAG29292.1};
GN   Synonyms=odhA {ECO:0000313|EMBL:BAG29292.1};
GN   OrderedLocusNames=KRH_09450 {ECO:0000313|EMBL:BAG29292.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG29292.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG29292.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000256|ARBA:ARBA00052761};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) =
CC         N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20092,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00051911};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC       CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004813}.
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DR   EMBL; AP009152; BAG29292.1; -; Genomic_DNA.
DR   RefSeq; WP_012398013.1; NC_010617.1.
DR   AlphaFoldDB; B2GLV1; -.
DR   STRING; 378753.KRH_09450; -.
DR   KEGG; krh:KRH_09450; -.
DR   eggNOG; COG0508; Bacteria.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_11; -.
DR   OMA; AAANKMC; -.
DR   OrthoDB; 9759785at2; -.
DR   UniPathway; UPA00223; UER00997.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:TreeGrafter.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR031717; ODO-1/KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   NCBIfam; NF006914; PRK09404.1; 1.
DR   NCBIfam; NF008907; PRK12270.1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAG29292.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          934..1127
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          45..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..83
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1274 AA;  140131 MW;  2F6D90EED8D9221B CRC64;
     MPDQPHHLIP EEFAGNEWLV DELFEKYQAD KNSVDKKWWP IFEQMAAEDG TPAPETARER
     PAASTTPAPA ARKSSAPAAA KTPQKADRAQ SPAPAATGAK AKGRPEGVDT EADSPEGSAT
     KRPIRAQPED RKEDTPAKAP EKPAEDKVVK LRGPAKAVAA NMDASLSVPT ATTVRAVPAK
     LLIDNRMVIN SHLARNRGGK VSFTHLVGYA VIRALSSFPS MNVVYDESDG KPAAIHPAHV
     NFGIAIDIPN KDGSRNLVVP NIKGAETMSF QEFWTSYEDI VKRGRNGALT MEDYSGTTVS
     LTNPGGIGTV HSVPRLSKGQ ACIIGVGALD YPAEYKGASP RTIARNAVSK VITLTSTYDH
     RVIQGAGSGE FLKLVEHYLL GGDDFYDHIF EALRIPYEPV RWAVDNQVNP EIQINKVARI
     QQLIHSYRVR GHLMADTNPL EYVMRKHPDL DIRTYGLTLW DLEREWPTGG FGGQNLLTLR
     VILGRLRDAY CRTVGVEYMH IQEPEQREWF QSKLERDYQK PSREEQFHIL ERLNAAEAFE
     TFLQTKYVGQ KRFSLEGGES LIPLLDAIMS EAADASLAGV GIAMAHRGRL NVLTNIAGKS
     YAQVFREFEG SQDPRAAEGS GDVKYHLGTE GVFTSDNGNE TQVYLAANPS HLEAADPVIE
     GIARAKTDVL GAGPEGDGEF PVLPIQVHGD AAMAGQGIVY EVMQMSGLEG YTVGGTIHVV
     VNNQVGFTTA PSAGRTSTYS TDVARTVQAP IFHVNADDPE AVTRVAQLAF EYRQRFHHDV
     VIDLVCYRRR GHNEGDDPSM TQPLMYSLID GKRSTRKVYT ENLVGRGDIT QEEADRALKD
     YQERLERVFA ETHEAQTSTV PLVTGDAAAI ANIERPSAQQ ADSGVSVPKS TAISPETAQR
     IGDAYVQMPE GFTMHRKLKK LAEKRRDMTR EGGIDWGMGE LMAFGSVLMD GVPVRMSGQD
     VRRGTFTQRQ AVFFDAENGA EWTPLNNLSA DQAHFSIYNS LLSEYGVLGF EYGYSVERPE
     ALTVWEAQFG DFTNGAQTIV DEFISSAEQK WGQRSNLVLL LPHGFEGQGP DHSSARIERF
     LTLCAEKNMI VAQPSTPANH FHLLRRQAYS RPRRPLIVAT PKQLLRLKAA ASPVEEFTQG
     GFQTVIPDTA GLDDAKVTDV ILVSGRLYYD LVTQRKNSDD HSTAIVRVEQ LYPLPVDEIK
     EQLARYPEAR ILWAQDEPAN QGAWPFMAVN LVPQLDRPVT LASRPASASP ANGSAKRHAA
     ELETLVQQAF DRGE
//